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Tyrosine-protein kinase BAZ1B (EC 2.7.10.2) (Bromodomain adjacent to zinc finger domain protein 1B) (Williams syndrome transcription factor homolog) (Williams-Beuren syndrome chromosomal region 9 protein homolog)

 BAZ1B_MOUSE             Reviewed;        1479 AA.
Q9Z277; B9EJ99; Q3URP5; Q3USR7; Q3UVM2; Q8CAU9; Q9CU68;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
30-AUG-2017, entry version 144.
RecName: Full=Tyrosine-protein kinase BAZ1B;
EC=2.7.10.2;
AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B;
AltName: Full=Williams syndrome transcription factor homolog;
AltName: Full=Williams-Beuren syndrome chromosomal region 9 protein homolog;
Name=Baz1b; Synonyms=Wbscr9, Wstf;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9858827;
Peoples R.J., Cisco M.J., Kaplan P., Francke U.;
"Identification of the WBSCR9 gene, encoding a novel transcriptional
regulator, in the Williams-Beuren syndrome deletion at 7q11.23.";
Cytogenet. Cell Genet. 82:238-246(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-810 AND 823-1799 (ISOFORM
1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786 (ISOFORM 2).
STRAIN=C57BL/6J;
TISSUE=Corpora quadrigemina, Thymus, and Urinary bladder;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION, AND INTERACTION WITH MYO1C.
PubMed=16514417; DOI=10.1038/sj.embor.7400657;
Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G.,
Krueger T., Thyberg J., Scheer U., Grummt I.,
Oestlund Farrants A.-K.O.;
"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear
myosin 1 and has a role in RNA polymerase I transcription.";
EMBO Rep. 7:525-530(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-1464, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SMARCA5.
PubMed=19092802; DOI=10.1038/nature07668;
Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,
Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,
Hofmann K., Patel D.J., Elledge S.J., Allis C.D.;
"WSTF regulates the H2A.X DNA damage response via a novel tyrosine
kinase activity.";
Nature 457:57-62(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-158; SER-161;
SER-325; SER-706; SER-709; SER-1464; SER-1466 AND SER-1468, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1331, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Atypical tyrosine-protein kinase that plays a central
role in chromatin remodeling and acts as a transcription
regulator. Involved in DNA damage response by phosphorylating
'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central
role in DNA repair and acts as a mark that distinguishes between
apoptotic and repair responses to genotoxic stress. Essential
component of the WICH complex, a chromatin remodeling complex that
mobilizes nucleosomes and reconfigures irregular chromatin to a
regular nucleosomal array structure. The WICH complex regulates
the transcription of various genes, has a role in RNA polymerase I
and RNA polymerase III transcription, mediates the histone H2AX
phosphorylation at 'Tyr-142', and is involved in the maintenance
of chromatin structures during DNA replication processes. In the
complex, it mediates the recruitment of the WICH complex to
replication foci during DNA replication. {ECO:0000250,
ECO:0000269|PubMed:16514417}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with MYO1C (By similarity). Interacts with
CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and
forms the WICH complex. Component of the B-WICH complex, at least
composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6,
MYBBP1A and DDX21. Interacts with VDR; in a ligand-dependent
manner. Interacts with PCNA; the interaction is direct (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q91ZW3:Smarca5; NbExp=2; IntAct=EBI-927576, EBI-927547;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475}.
Note=Accumulates in pericentromeric heterochromatin during
replication. Targeted to replication foci throughout S phase via
its association with PCNA (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z277-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z277-2; Sequence=VSP_037470;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Expressed as early as day 7 and in equal
amounts during gestation.
-!- DOMAIN: The N-terminal part, including the WAC domain and the C
motif, mediates the tyrosine-protein kinase activity.
{ECO:0000250}.
-!- DOMAIN: The bromo domain mediates the specific interaction with
acetylated histones. {ECO:0000250}.
-!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily.
{ECO:0000305}.
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EMBL; AF084480; AAD08676.1; -; mRNA.
EMBL; CH466529; EDL19376.1; -; Genomic_DNA.
EMBL; BC141399; AAI41400.1; -; mRNA.
EMBL; AK017894; BAB30992.1; -; mRNA.
EMBL; AK037737; BAC29862.1; -; mRNA.
EMBL; AK137139; BAE23247.1; -; mRNA.
EMBL; AK140172; BAE24264.1; -; mRNA.
EMBL; AK141305; BAE24643.1; -; mRNA.
CCDS; CCDS19736.1; -. [Q9Z277-1]
PIR; T17401; T17401.
RefSeq; NP_035844.2; NM_011714.2. [Q9Z277-1]
RefSeq; XP_011239182.1; XM_011240880.2. [Q9Z277-2]
UniGene; Mm.40331; -.
ProteinModelPortal; Q9Z277; -.
SMR; Q9Z277; -.
BioGrid; 204552; 3.
DIP; DIP-36072N; -.
IntAct; Q9Z277; 3.
MINT; MINT-4089121; -.
STRING; 10090.ENSMUSP00000002825; -.
iPTMnet; Q9Z277; -.
PhosphoSitePlus; Q9Z277; -.
EPD; Q9Z277; -.
PaxDb; Q9Z277; -.
PeptideAtlas; Q9Z277; -.
PRIDE; Q9Z277; -.
Ensembl; ENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748. [Q9Z277-1]
GeneID; 22385; -.
KEGG; mmu:22385; -.
UCSC; uc008zxz.2; mouse. [Q9Z277-1]
CTD; 9031; -.
MGI; MGI:1353499; Baz1b.
eggNOG; KOG1245; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119099; -.
HOVERGEN; HBG050668; -.
InParanoid; Q9Z277; -.
KO; K11658; -.
OMA; HPQGIRE; -.
OrthoDB; EOG091G00KF; -.
PhylomeDB; Q9Z277; -.
TreeFam; TF106397; -.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
ChiTaRS; Baz1b; mouse.
PRO; PR:Q9Z277; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000002748; -.
CleanEx; MM_BAZ1B; -.
Genevisible; Q9Z277; MM.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0043596; C:nuclear replication fork; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0035173; F:histone kinase activity; ISS:UniProtKB.
GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0071884; F:vitamin D receptor activator activity; IMP:BHF-UCL.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:MGI.
GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:BHF-UCL.
GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
GO; GO:0016572; P:histone phosphorylation; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR001487; Bromodomain.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR018501; DDT_dom.
InterPro; IPR028942; WHIM1_dom.
InterPro; IPR028941; WHIM2_dom.
InterPro; IPR013136; WSTF_Acf1_Cbp146.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
Pfam; PF15612; WHIM1; 1.
Pfam; PF15613; WSD; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SMART; SM00571; DDT; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50827; DDT; 1.
PROSITE; PS51136; WAC; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Bromodomain;
Coiled coil; Complete proteome; DNA damage; Isopeptide bond; Kinase;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Transferase; Tyrosine-protein kinase; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 1479 Tyrosine-protein kinase BAZ1B.
/FTId=PRO_0000211171.
DOMAIN 20 126 WAC. {ECO:0000255|PROSITE-
ProRule:PRU00475}.
DOMAIN 605 669 DDT. {ECO:0000255|PROSITE-
ProRule:PRU00063}.
DOMAIN 1352 1422 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
ZN_FING 1184 1234 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 1 345 Mediates the tyrosine-protein kinase
activity. {ECO:0000250}.
COILED 537 587 {ECO:0000255}.
COILED 774 809 {ECO:0000255}.
COILED 854 890 {ECO:0000255}.
COILED 1257 1284 {ECO:0000255}.
MOTIF 207 213 C motif.
COMPBIAS 306 579 Lys-rich.
MOD_RES 152 152 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 706 706 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 709 709 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 1315 1315 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 1331 1331 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1338 1338 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UIG0}.
MOD_RES 1464 1464 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1466 1466 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1468 1468 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 827 827 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q9UIG0}.
CROSSLNK 827 827 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIG0}.
CROSSLNK 854 854 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIG0}.
CROSSLNK 1043 1043 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIG0}.
CROSSLNK 1089 1089 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIG0}.
CROSSLNK 1107 1107 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9UIG0}.
VAR_SEQ 1 298 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_037470.
CONFLICT 957 957 S -> R (in Ref. 1; AAD08676).
{ECO:0000305}.
CONFLICT 1017 1017 L -> F (in Ref. 1; AAD08676).
{ECO:0000305}.
CONFLICT 1031 1034 SIYL -> CNYM (in Ref. 1; AAD08676).
{ECO:0000305}.
SEQUENCE 1479 AA; 170651 MW; 6EFBF3913EA93AF0 CRC64;
MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL
THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE KLVDSAWLEI MTKYAVGEEC
DFEVGKEKML KVKIVKIHPL EKVDEEAVEK KSDGACDSPS SDKENSSQMA QDLQKKETVV
KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS
LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP LKVKNSKNSK
SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD KPLKAKGRGK GILNGQKSTG
NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK MTRTPRSSGG VPRSSGKPHK HLPPAALHLI
AYYKENKDKE DKKSALSCVI SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS
EEQRKEYLKK KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP
EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL YLNRVLVILL
QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC DVQEDSEGSE TDDNKDSTPF
EDNEVQDEFL EKLETSEFFE LTSEEKLRIL TALCHRILMT YSVQDHMETR QQVSAELWKE
RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI
SAVKSRRLLS MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR
RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD DDYCPRSKKA
NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL DELLSCLHPQ GIRESQLKER
LEKRYQEITH SIYLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYMEGTSEF
EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV
EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI
LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST SEGSEGDESG
EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR PGRPPGKKSH PARRSRPKDD
PEVDDLVLQT KRISRRQSLE LQKCEDILHK LVKYRFSWPF REPVTRDEAE DYYDVIEHPM
DFQTIQNKCS CGNYRSVQEF LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL
PGHPYVRRKR RKFPDRLADD EGDSDSESVG QSRGRRQKK


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CN043_HUMAN Mouse ELISA Kit FOR Williams-Beuren syndrome chromosomal region 16 protein homolog 96T
HXA5_RAT Mouse ELISA Kit FOR Williams-Beuren syndrome chromosomal region 16 protein homolog 96T
EIAAB11357 DnaJ homolog subfamily C member 30,Dnajc30,Mouse,Mus musculus,Wbscr18,Williams-Beuren syndrome chromosomal region 18 protein homolog
EIAAB46118 Mouse,Mus musculus,Wbscr28,Williams-Beuren syndrome chromosomal region 28 protein homolog
EIAAB46119 Bos taurus,Bovine,WBSCR28,Williams-Beuren syndrome chromosomal region 28 protein homolog
EIAAB46111 Mouse,Mus musculus,Wbscr16,Williams-Beuren syndrome chromosomal region 16 protein homolog
EIAAB24975 Carbohydrate-responsive element-binding protein,ChREBP,Mio,MLX interactor,MLX-interacting protein-like,Mlxipl,Mouse,Mus musculus,Wbscr14,Williams-Beuren syndrome chromosomal region 14 protein homolog
EIAAB11356 DnaJ homolog subfamily C member 30,DNAJC30,Homo sapiens,Human,WBSCR18,Williams-Beuren syndrome chromosomal region 18 protein
EIAAB27991 Mouse,Mus musculus,NOL1_NOP2_Sun domain family member 5,Nsun5,Putative methyltransferase NSUN5,Wbscr20,Wbscr20a,Williams-Beuren syndrome chromosomal region 20A protein homolog
EIAAB46115 Mouse,Mus musculus,Uncharacterized methyltransferase WBSCR22,Wbscr22,Williams-Beuren syndrome chromosomal region 22 protein homolog
EIAAB46114 Bos taurus,Bovine,Uncharacterized methyltransferase WBSCR22,WBSCR22,Williams-Beuren syndrome chromosomal region 22 protein homolog
18-003-42110 General transcription factor II-I - GTFII-I; TFII-I; Bruton tyrosine kinase-associated protein 135; BTK-associated protein 135; BAP-135; SRF-Phox1-interacting protein; SPIN; Williams-Beuren syndrome c 0.1 mg Protein A
18-003-42110 General transcription factor II-I - GTFII-I; TFII-I; Bruton tyrosine kinase-associated protein 135; BTK-associated protein 135; BAP-135; SRF-Phox1-interacting protein; SPIN; Williams-Beuren syndrome c 0.05 mg Aff Pur
EIAAB46112 Homo sapiens,Human,RCC1-like G exchanging factor-like protein,WBSCR16,Williams-Beuren syndrome chromosomal region 16 protein
I2785 Williams-Beuren syndrome chromosomal region 27 protein (WBSCR27), Human, ELISA Kit 96T
I2783 Williams-Beuren syndrome chromosomal region 16 protein (WBSCR16), Human, ELISA Kit 96T
CSB-EL025989HU Human Williams-Beuren syndrome chromosomal region 28 protein(WBSCR28) ELISA kit 96T
I2787 Williams-Beuren syndrome chromosomal region 28 protein (WBSCR28), Human, ELISA Kit 96T
I2784 Williams-Beuren syndrome chromosomal region 16 protein (WBSCR16), Mouse, ELISA Kit 96T
I2786 Williams-Beuren syndrome chromosomal region 28 protein (WBSCR28), Bovine, ELISA Kit 96T
CSB-EL014645HU Human Williams-Beuren syndrome chromosomal region 14 protein(MLXIPL) ELISA kit 96T
CSB-EL025981HU Human Williams-Beuren syndrome chromosomal region 16 protein(WBSCR16) ELISA kit 96T
CSB-EL025988HU Human Williams-Beuren syndrome chromosomal region 27 protein(WBSCR27) ELISA kit 96T
WBS23_HUMAN Human ELISA Kit FOR Putative Williams-Beuren syndrome chromosomal region 23 protein 96T


 

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